Aminopeptidase B
Aminopeptidase B (EC 3.4.11.6, arylamidase II, arginine aminopeptidase, arginyl aminopeptidase, Cl—activated arginine aminopeptidase, cytosol aminopeptidase IV, L-arginine aminopeptidase) is an enzyme.[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction
- Release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys
Aminopeptidase B | |||||||||
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Identifiers | |||||||||
EC no. | 3.4.11.6 | ||||||||
CAS no. | 9073-92-1 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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This enzyme from mammalian tissues is activated by chloride ions and low concentrations of thiol compounds.
An inhibitor is bestatin (ubenimex).
References
- Gainer H, Russell JT, Loh YP (September 1984). "An aminopeptidase activity in bovine pituitary secretory vesicles that cleaves the N-terminal arginine from beta-lipotropin60-65". FEBS Letters. 175 (1): 135–9. doi:10.1016/0014-5793(84)80586-4. PMID 6434344.
- Belhacene N, Mari B, Rossi B, Auberger P (August 1993). "Characterization and purification of T lymphocyte aminopeptidase B: a putative marker of T cell activation". European Journal of Immunology. 23 (8): 1948–55. doi:10.1002/eji.1830230833. PMID 8344358. S2CID 855382.
- Cadel S, Pierotti AR, Foulon T, Créminon C, Barré N, Segrétain D, Cohen P (April 1995). "Aminopeptidase-B in the rat testes: isolation, functional properties and cellular localization in the seminiferous tubules". Molecular and Cellular Endocrinology. 110 (1–2): 149–60. doi:10.1016/0303-7207(95)03529-g. PMID 7672445. S2CID 6951437.
- Fukasawa KM, Fukasawa K, Kanai M, Fujii S, Harada M (November 1996). "Molecular cloning and expression of rat liver aminopeptidase B". The Journal of Biological Chemistry. 271 (48): 30731–5. doi:10.1074/jbc.271.48.30731. PMID 8940051.
- Cadel S, Foulon T, Viron A, Balogh A, Midol-Monnet S, Noël N, Cohen P (April 1997). "Aminopeptidase B from the rat testis is a bifunctional enzyme structurally related to leukotriene-A4 hydrolase". Proceedings of the National Academy of Sciences of the United States of America. 94 (7): 2963–8. Bibcode:1997PNAS...94.2963C. doi:10.1073/pnas.94.7.2963. PMC 20305. PMID 9096329.
- Orning L, Gierse JK, Fitzpatrick FA (April 1994). "The bifunctional enzyme leukotriene-A4 hydrolase is an arginine aminopeptidase of high efficiency and specificity". The Journal of Biological Chemistry. 269 (15): 11269–73. doi:10.1016/S0021-9258(19)78120-4. PMID 8157657.
External links
- Aminopeptidase+B at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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